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6ZIB

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH ACETOACETYL-COA AND NADH

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003824molecular_functioncatalytic activity
AAA0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
AAA0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
AAA0004300molecular_functionenoyl-CoA hydratase activity
AAA0005777cellular_componentperoxisome
AAA0005782cellular_componentperoxisomal matrix
AAA0005829cellular_componentcytosol
AAA0006629biological_processlipid metabolic process
AAA0006631biological_processfatty acid metabolic process
AAA0006633biological_processfatty acid biosynthetic process
AAA0006635biological_processfatty acid beta-oxidation
AAA0016491molecular_functionoxidoreductase activity
AAA0016509molecular_functionlong-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
AAA0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
AAA0016829molecular_functionlyase activity
AAA0016853molecular_functionisomerase activity
AAA0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
AAA0018812molecular_function3-hydroxyacyl-CoA dehydratase activity
AAA0019899molecular_functionenzyme binding
AAA0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
AAA0070403molecular_functionNAD+ binding
BBB0003824molecular_functioncatalytic activity
BBB0003857molecular_function(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
BBB0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
BBB0004300molecular_functionenoyl-CoA hydratase activity
BBB0005777cellular_componentperoxisome
BBB0005782cellular_componentperoxisomal matrix
BBB0005829cellular_componentcytosol
BBB0006629biological_processlipid metabolic process
BBB0006631biological_processfatty acid metabolic process
BBB0006633biological_processfatty acid biosynthetic process
BBB0006635biological_processfatty acid beta-oxidation
BBB0016491molecular_functionoxidoreductase activity
BBB0016509molecular_functionlong-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
BBB0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
BBB0016829molecular_functionlyase activity
BBB0016853molecular_functionisomerase activity
BBB0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
BBB0018812molecular_function3-hydroxyacyl-CoA dehydratase activity
BBB0019899molecular_functionenzyme binding
BBB0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
BBB0070403molecular_functionNAD+ binding
Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG
ChainResidueDetails
AAAASN474-GLY498

site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY
ChainResidueDetails
AAALEU90-TYR110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues560
DetailsRegion: {"description":"Enoyl-CoA hydratase / isomerase"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Blocked amino end (Ala)"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q08426","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q08426","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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